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Conserved domains on  [gi|1050115330|ref|NP_001316800|]
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astrocytic phosphoprotein PEA-15 isoform 3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DD super family cl14633
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
 2-63 6.58e-28

Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) superfamily includes the DD, Pyrin, CARD (Caspase activation and recruitment domain) and DED (Death Effector Domain) families. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. They are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways including those that impact innate immunity, inflammation, differentiation, and cancer.


The actual alignment was detected with superfamily member cd08338:

Pssm-ID: 472698  Cd Length: 84  Bit Score: 97.14  E-value: 6.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115330   2 AEYGTLLQDLTNNITLEDLEQLKSACKEDIPSEK----------------------NNLSYIEHIFEISRRPDLLTMVVD 59
Cdd:cd08338     1 GEYGSLLQDLTENITSEDLEQLKSACKEDIPSEKseeittgsawfsflekhnkldqDNLSYIEHVFEISRRPDLLTMVVD 80


                  ....
gi 1050115330  60 YRTR 63
Cdd:cd08338    81 YRTK 84
 
Name Accession Description Interval E-value
DED_PEA15 cd08338
Death Effector Domain of Astrocyte phosphoprotein PEA-15; Death Effector Domain (DED) similar ...
 2-63 6.58e-28

Death Effector Domain of Astrocyte phosphoprotein PEA-15; Death Effector Domain (DED) similar to that found in PEA-15 (Astrocyte phosphoprotein PEA-15). PEA-15 is a multifunctional phosphoprotein that modulates signaling pathways, like the ERK MAP kinase cascade by binding to ERK and changing its subcellular localization. It has been implicated in apoptosis, cell proliferation, and glucose metabolism. It does not possess enzymatic activity and mainly acts as an adaptor protein. PEA-15 contains an N-terminal DED domain and a C-terminal disordered region. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.


Pssm-ID: 260045  Cd Length: 84  Bit Score: 97.14  E-value: 6.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115330   2 AEYGTLLQDLTNNITLEDLEQLKSACKEDIPSEK----------------------NNLSYIEHIFEISRRPDLLTMVVD 59
Cdd:cd08338     1 GEYGSLLQDLTENITSEDLEQLKSACKEDIPSEKseeittgsawfsflekhnkldqDNLSYIEHVFEISRRPDLLTMVVD 80


                  ....
gi 1050115330  60 YRTR 63
Cdd:cd08338    81 YRTK 84
DED smart00031
Death effector domain;
2-59 4.71e-09

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 48.82  E-value: 4.71e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1050115330    2 AEYGTLLQDLTNNITLEDLEQLKSACKEDIPSEK---------------------NNLSYIEHIFEISRRPDLLTMVVD 59
Cdd:smart00031   1 SPYRVLLLLISEELDSEELEVLLFLCKDLIPKRKleiktfldlfsaleeqgllseDNLSLLAELLYRLRRLDLLRRLFG 79
DED pfam01335
Death effector domain;
4-63 1.21e-06

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 42.85  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115330   4 YGTLLQDLTNNITLEDLEQLKSACKEDIPSEK----------------------NNLSYIEHIFEISRRPDLLTMVVDYR 61
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKlekiksaldlfielekqgllseDNLDLLEELLRRIGRQDLLKKIEKYE 80


                  ..
gi 1050115330  62 TR 63
Cdd:pfam01335  81 RE 82
 
Name Accession Description Interval E-value
DED_PEA15 cd08338
Death Effector Domain of Astrocyte phosphoprotein PEA-15; Death Effector Domain (DED) similar ...
 2-63 6.58e-28

Death Effector Domain of Astrocyte phosphoprotein PEA-15; Death Effector Domain (DED) similar to that found in PEA-15 (Astrocyte phosphoprotein PEA-15). PEA-15 is a multifunctional phosphoprotein that modulates signaling pathways, like the ERK MAP kinase cascade by binding to ERK and changing its subcellular localization. It has been implicated in apoptosis, cell proliferation, and glucose metabolism. It does not possess enzymatic activity and mainly acts as an adaptor protein. PEA-15 contains an N-terminal DED domain and a C-terminal disordered region. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.


Pssm-ID: 260045  Cd Length: 84  Bit Score: 97.14  E-value: 6.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115330   2 AEYGTLLQDLTNNITLEDLEQLKSACKEDIPSEK----------------------NNLSYIEHIFEISRRPDLLTMVVD 59
Cdd:cd08338     1 GEYGSLLQDLTENITSEDLEQLKSACKEDIPSEKseeittgsawfsflekhnkldqDNLSYIEHVFEISRRPDLLTMVVD 80


                  ....
gi 1050115330  60 YRTR 63
Cdd:cd08338    81 YRTK 84
DD cd08304
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
 8-57 2.33e-12

Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) superfamily includes the DD, Pyrin, CARD (Caspase activation and recruitment domain) and DED (Death Effector Domain) families. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. They are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways including those that impact innate immunity, inflammation, differentiation, and cancer.


Pssm-ID: 176720  Cd Length: 69  Bit Score: 57.18  E-value: 2.33e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1050115330   8 LQDLTNNITLEDLEQLKSACKEDIPSEK-------------------NNLSYIEHIFEISRRPDLLTMV 57
Cdd:cd08304     1 RLDLCENLTLEVLQQLKTALKSRIPPDQveqisaanellnilesqynHTLQLLFALFEDLGLHNLARLL 69
DED smart00031
Death effector domain;
2-59 4.71e-09

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 48.82  E-value: 4.71e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1050115330    2 AEYGTLLQDLTNNITLEDLEQLKSACKEDIPSEK---------------------NNLSYIEHIFEISRRPDLLTMVVD 59
Cdd:smart00031   1 SPYRVLLLLISEELDSEELEVLLFLCKDLIPKRKleiktfldlfsaleeqgllseDNLSLLAELLYRLRRLDLLRRLFG 79
DED cd00045
Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a ...
 4-58 6.51e-09

Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a subfamily of the Death Domain (DD) superfamily. DED-containing proteins include Fas-Associated via Death Domain (FADD), Astrocyte phosphoprotein PEA-15, the initiator caspases (caspase-8 and -10), and FLICE-inhibitory protein (FLIP), among others. These proteins are prominent components of the programmed cell death (apoptosis) pathway. Some members also have non-apoptotic functions such as regulation of insulin signaling (DEDD and PEA15) and cell cycle progression (DEDD). DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.


Pssm-ID: 260016  Cd Length: 77  Bit Score: 48.35  E-value: 6.51e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1050115330   4 YGTLLQDLTNNITLEDLEQLKSACKEDIPS----------------------EKNNLSYIEHIFEISRRPDLLTMVV 58
Cdd:cd00045     1 YRQLLLKISDELTSEELRSLKFLCKDVIPAgklerisrgrdlftelekqgkiSPGNLSLLEELLRSIGRRDLLEKVE 77
DED pfam01335
Death effector domain;
4-63 1.21e-06

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 42.85  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115330   4 YGTLLQDLTNNITLEDLEQLKSACKEDIPSEK----------------------NNLSYIEHIFEISRRPDLLTMVVDYR 61
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKlekiksaldlfielekqgllseDNLDLLEELLRRIGRQDLLKKIEKYE 80


                  ..
gi 1050115330  62 TR 63
Cdd:pfam01335  81 RE 82
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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